Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

EBNA1-Mediated Recruitment of a Histone H2B Deubiquitylating Complex to the Epstein-Barr Virus Latent Origin of DNA Replication

15 Oct 2009

Abstract excerpt

The EBNA1 protein of Epstein-Barr virus (EBV) plays essential roles in enabling the replication and persistence of EBV genomes in latently infected cells and activating EBV latent gene expression, in all cases by binding to specific recognition sites in the latent origin of replication, oriP. Here we show that EBNA1 binding to its recognition sites in vitro is greatly stimulated by binding to the cellular...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytomegalovirus and herpesvirus research
Share to Histiocytic Disorders and Treatments
Share to Viral-associated cancers and disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19834552
DOI: 10.1371/journal.ppat.1000624

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

EBNA1-Mediated Recruitment of a Histone H2B Deubiquitylating Complex to the Epstein-Barr Virus Latent Origin of DNA ReplicationPMID 19834552Read ↗

USP7 inhibitors disrupt EBNA1 interactome and EBV tumorigenesisSemantic proximity Read ↗

USP7 Inhibitors Destabilize EBNA1 and Suppress Epstein‐Barr Virus TumorigenesisSemantic proximity Read ↗

Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7.Semantic proximity Read ↗

Human Cytomegalovirus UL138 Interaction with USP1 Activates STAT1 in infectionSemantic proximity Read ↗

The Ubiquitin-Specific Protease Usp7, a Novel Merkel Cell Polyomavirus Large T-Antigen Interaction Partner, Modulates Viral DNA ReplicationSemantic proximity Read ↗

Regulation of EBNA1 protein stability and DNA replication activity by PLOD1 lysine hydroxylaseSemantic proximity Read ↗

GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7.Semantic proximity Read ↗

B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription.Semantic proximity Read ↗

Regulation of EBNA1 Protein Stability by PLOD1 Lysine HydroxylaseSemantic proximity Read ↗

Epstein-Barr virus deubiquitinating enzyme BPLF1 is involved in EBV carcinogenesis by affecting cellular genomic stabilitySemantic proximity Read ↗

The dimeric deubiquitinase USP28 integrates 53BP1 and MYC functions to limit DNA damageSemantic proximity Read ↗

The Nuclear Chaperone Nucleophosmin Escorts an Epstein-Barr Virus Nuclear Antigen to Establish Transcriptional Cascades for Latent Infection in Human B CellsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.